For a detailed overview of current projects, links to abstracts of recent papers, and a list of references, go to my Lab Home Page
Protein folding, protein structure/function relationships, protein-protein interactions and the mechanism of enzymatic reactions are projects currently under study in this laboratory.
The long term goal of the protein folding studies is to understand the nature of the intermediate structures on the unfolding and refolding pathways, including the role of proteins that assist folding (called chaperonins). The work uses site-directed mutagenesis and techniques such as 19F and proton NMR, circular dichroism, fluorescence measurements and x-ray crystallography. Proteins in these studies include the intestinal fatty acid binding protein, dihydrofolate reductase, actin, and GroEL.
Studies on protein-protein interactions are related to the folding studies but also include actin, actin binding proteins and polymerization processes. The long term goal of this work is to understand the role of actin in maintaining the cytoskeletal structure of cells and how such structures control cellular functions. Studies on site-directed mutants of actin are underway.
The long term goal of kinetic studies with enzymes is to understand the catalytic mechanism of specific enzymatic reactions.
URL: http://biochem.wustl.edu/~frieden
last update: $Date: 1996/08/13$